RSGA_ECOL6
ID RSGA_ECOL6 Reviewed; 350 AA.
AC Q8FAL3;
DT 31-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2003, sequence version 2.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Small ribosomal subunit biogenesis GTPase RsgA {ECO:0000255|HAMAP-Rule:MF_01820};
DE EC=3.6.1.- {ECO:0000255|HAMAP-Rule:MF_01820};
GN Name=rsgA {ECO:0000255|HAMAP-Rule:MF_01820}; OrderedLocusNames=c5248;
OS Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=199310;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CFT073 / ATCC 700928 / UPEC;
RX PubMed=12471157; DOI=10.1073/pnas.252529799;
RA Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D.,
RA Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F.,
RA Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T.,
RA Donnenberg M.S., Blattner F.R.;
RT "Extensive mosaic structure revealed by the complete genome sequence of
RT uropathogenic Escherichia coli.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002).
CC -!- FUNCTION: One of several proteins that assist in the late maturation
CC steps of the functional core of the 30S ribosomal subunit. Helps
CC release RbfA from mature subunits. May play a role in the assembly of
CC ribosomal proteins into the subunit. Circularly permuted GTPase that
CC catalyzes slow GTP hydrolysis, GTPase activity is stimulated by the 30S
CC ribosomal subunit. {ECO:0000255|HAMAP-Rule:MF_01820}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01820};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP-Rule:MF_01820};
CC -!- SUBUNIT: Monomer. Associates with 30S ribosomal subunit, binds 16S
CC rRNA. {ECO:0000255|HAMAP-Rule:MF_01820}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01820}.
CC -!- SIMILARITY: Belongs to the TRAFAC class YlqF/YawG GTPase family. RsgA
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_01820}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAN83670.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AE014075; AAN83670.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_000041976.1; NC_004431.1.
DR AlphaFoldDB; Q8FAL3; -.
DR SMR; Q8FAL3; -.
DR STRING; 199310.c5248; -.
DR EnsemblBacteria; AAN83670; AAN83670; c5248.
DR KEGG; ecc:c5248; -.
DR eggNOG; COG1162; Bacteria.
DR HOGENOM; CLU_033617_2_0_6; -.
DR OMA; CLVAAYD; -.
DR Proteomes; UP000001410; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-KW.
DR GO; GO:0042274; P:ribosomal small subunit biogenesis; IEA:UniProtKB-UniRule.
DR CDD; cd01854; YjeQ_EngC; 1.
DR Gene3D; 2.40.50.140; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_01820; GTPase_RsgA; 1.
DR InterPro; IPR030378; G_CP_dom.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR004881; Ribosome_biogen_GTPase_RsgA.
DR InterPro; IPR010914; RsgA_GTPase_dom.
DR PANTHER; PTHR32120; PTHR32120; 1.
DR Pfam; PF03193; RsgA_GTPase; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00157; TIGR00157; 1.
DR PROSITE; PS50936; ENGC_GTPASE; 1.
DR PROSITE; PS51721; G_CP; 1.
PE 3: Inferred from homology;
KW Cytoplasm; GTP-binding; Hydrolase; Metal-binding; Nucleotide-binding;
KW Ribosome biogenesis; RNA-binding; rRNA-binding; Zinc.
FT CHAIN 1..350
FT /note="Small ribosomal subunit biogenesis GTPase RsgA"
FT /id="PRO_0000008151"
FT DOMAIN 104..273
FT /note="CP-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01058"
FT REGION 1..33
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 160..163
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01820"
FT BINDING 214..222
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01820"
FT BINDING 297
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01820"
FT BINDING 302
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01820"
FT BINDING 304
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01820"
FT BINDING 310
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01820"
SQ SEQUENCE 350 AA; 39237 MW; 06D791587F522C18 CRC64;
MSKNKLSKGQ QRRVNANHQR RLKTSKEKPD YDDNLFGEPD EGIVISRFGM HADVESADGD
VHRCNIRRTI RSLVTGDRVV WRPGKPAAEG VNVKGIVEAV HERTSVLTRP DFYDGVKPIA
ANIDQIVIVS AILPELSLNI IDRYLVACET LQIEPIIVLN KIDLLDDEGM EFVNEQMDIY
RNIGYRVLMV SSHTQDGLKP LEEALTGRIS IFAGQSGVGK SSLLNALLGL QKEILTNDVS
DNSGLGQHTT TAARLYHFPH GGDVIDSPGV REFGLWHLEP EQITQGFVEF HDYLGLCKYR
DCKHDTDPGC AIREAVEEGK IAETRFENYH RILESMAQVK TRKNFSDTDD
